Biochem - Lecture 3 Learning Objectives

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primary protein structure

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all of the learning objectives and key concepts for the third lecture on amino acids, linked functions, and peptide bonds

biochemistry

35 Terms

1

primary protein structure

sequence of amino acids in protein

<p>sequence of amino acids in protein</p>
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2

secondary protein structure

folds up into shapes

<p>folds up into shapes</p>
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3

tertiary protein structure

whole structure of protein

<p>whole structure of protein</p>
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4

quaternary protein structure

multiple proteins

<p>multiple proteins </p>
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5

amino acid residue

amino acid that is attached by a peptide bond to another amino acid

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6

backbone

the amino group, the carboxyl group, and the alpha carbon

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7

side chains

the R group unique to each amino acid

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8

disulfide bonds

also known as disulfide bridges. covalent bonds that form between the sulfur atoms of two cysteine amino acids in proteins

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9

conformation

the folded shape of the protein as determined by the amino acid sequence

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10

configuration

L or D. Most amino acids are L-isomers

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11

What is the difference between glutamate and glutamic acid?

glutamic acid has no charges and no net charge but if it undergoes a protonation-deprotonation reaction, it will produce glutamate, which contains multiple charges on it (same is true for other acids)

<p>glutamic acid has no charges and no net charge but if it undergoes a protonation-deprotonation reaction, it will produce glutamate, which contains multiple charges on it (same is true for other acids)</p>
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12

-ate means what?

conjugate base form of a carboxylic acid

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13

what are linked functions?

reactions that work together to maintain a cellular process

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14

peptide bond

chemical bond formed between two molecules when the carboxyl group of one molecule reacts with the amino group of the other molecule

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15

when does deprotonation occur?

when the compound is more acidic

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16

when does protonation occur?

when the compound is more basic

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17

what ionizable functional groups will deprotonate?

carboxyl group

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18

what ionizable functional groups will protonate?

amino group

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19

what amino acids deprotonate?

D, E, Y, R

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20

What amino acids protonate?

H, K, C

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21

what is the product of condensation of 2 amino acids?

dipeptide, which is a molecule formed by joining two amino acids through a peptide bond

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22

if pKa < pH the compound will

deprotonate

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23

if pKa > pH the compound will

protonate

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24

if pKa = pH the compound will

be equal parts protonated and deprotonated

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25

amino acids are ionizable because

their side chains can gain or lose electrons

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26

what pH are we using?

physiological pH = 7

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27

alpha carbonyl group will be

deprotonated

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28

alpha amino group will be

protonated

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29

aspartate (aspartic acid) will be

deprotonated

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30

glutamate (glutamic acid) will be

deprotonated

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31

histidine will be

deprotonated

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32

cysteine will be

protonated

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33

lysine will be

protonated

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34

tyrosine will be

protonated

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35

arginine will be

protonated

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